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Variable Control of Ets-1 DNA Binding by Multiple Phosphates in an Unstructured Region
- Source :
- Science. 309:142-145
- Publication Year :
- 2005
- Publisher :
- American Association for the Advancement of Science (AAAS), 2005.
-
Abstract
- Cell signaling that culminates in posttranslational modifications directs protein activity. Here we report how multiple Ca 2+ -dependent phosphorylation sites within the transcription activator Ets-1 act additively to produce graded DNA binding affinity. Nuclear magnetic resonance spectroscopic analyses show that phosphorylation shifts Ets-1 from a dynamic conformation poised to bind DNA to a well-folded inhibited state. These phosphates lie in an unstructured flexible region that functions as the allosteric effector of autoinhibition. Variable phosphorylation thus serves as a “rheostat” for cell signaling to fine-tune transcription at the level of DNA binding.
- Subjects :
- Models, Molecular
Protein Folding
Cell signaling
HMG-box
Protein Conformation
Molecular Sequence Data
Allosteric regulation
Biology
Protein Structure, Secondary
Proto-Oncogene Protein c-ets-1
Mice
chemistry.chemical_compound
Allosteric Regulation
Transcription (biology)
Proto-Oncogene Proteins
Animals
Amino Acid Sequence
Phosphorylation
Nuclear Magnetic Resonance, Biomolecular
Multidisciplinary
Proto-Oncogene Proteins c-ets
Activator (genetics)
DNA
Protein Structure, Tertiary
Cell biology
DNA binding site
Amino Acid Substitution
chemistry
Biochemistry
Calcium-Calmodulin-Dependent Protein Kinases
Mutation
Calcium-Calmodulin-Dependent Protein Kinase Type 2
Hydrophobic and Hydrophilic Interactions
Protein Binding
Signal Transduction
Transcription Factors
Subjects
Details
- ISSN :
- 10959203 and 00368075
- Volume :
- 309
- Database :
- OpenAIRE
- Journal :
- Science
- Accession number :
- edsair.doi.dedup.....244196419b1446b7867b5d096b7de02a
- Full Text :
- https://doi.org/10.1126/science.1111915